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Protein

Membrane-bound O-acyltransferase domain-containing protein 2

Gene

Mboat2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei341 – 3411By similarity
Active sitei372 – 3721By similarity

GO - Molecular functioni

  1. transferase activity, transferring acyl groups Source: UniProtKB-KW

GO - Biological processi

  1. phospholipid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_339882. Acyl chain remodelling of PE.
REACT_341560. Acyl chain remodelling of PC.
UniPathwayiUPA00085.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-bound O-acyltransferase domain-containing protein 2 (EC:2.3.-.-)
Short name:
O-acyltransferase domain-containing protein 2
Gene namesi
Name:Mboat2
Synonyms:Oact2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1305798. Mboat2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei22 – 4221HelicalSequence AnalysisAdd
BLAST
Transmembranei61 – 8121HelicalSequence AnalysisAdd
BLAST
Transmembranei88 – 10821HelicalSequence AnalysisAdd
BLAST
Transmembranei184 – 20421HelicalSequence AnalysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence AnalysisAdd
BLAST
Transmembranei288 – 30518HelicalSequence AnalysisAdd
BLAST
Transmembranei365 – 38521HelicalSequence AnalysisAdd
BLAST
Transmembranei415 – 43521HelicalSequence AnalysisAdd
BLAST
Transmembranei443 – 46321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519Membrane-bound O-acyltransferase domain-containing protein 2PRO_0000273022Add
BLAST

Proteomic databases

PaxDbiQ3T1J2.

Expressioni

Gene expression databases

ExpressionAtlasiQ3T1J2. baseline.
GenevestigatoriQ3T1J2.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009018.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5202.
HOGENOMiHOG000015994.
HOVERGENiHBG058823.
InParanoidiQ3T1J2.
KOiK13517.
OrthoDBiEOG73Z2SW.
PhylomeDBiQ3T1J2.
TreeFamiTF314906.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3T1J2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAV WFRTYLHSSK
60 70 80 90 100
TSSFIRHVVA TLLGLYLAFF CFGWYALHFL VQSGISYCIM IIAGVESMHQ
110 120 130 140 150
CCFVFALGYL SVCQITRVYI FDYGQYSADF SGPMMIITQK ITSLAYEIHD
160 170 180 190 200
GMFRKDEELT PSQRGLAVRR MPSLLEYVSY TCNFMGILAG PLCSYKDYIA
210 220 230 240 250
FIEGRASHMA QSGENGKEEQ HGKAEPSPNA AVTEKLLVCG LSLLFHLTIS
260 270 280 290 300
SMLPVEYNID EHFQATASWP TKATYLYVSL LAARPKYYFA WTLADAINNA
310 320 330 340 350
AGFGFRGYDK NGVARWDLIS NLRIQQIEMS TSFKMFLDNW NIQTALWLKR
360 370 380 390 400
VCYERATFSP TVQTFFLSAI WHGVYPGYYL TFLTGVLMTL AARAVRNNFR
410 420 430 440 450
HYFVEPPQLK LFYDIITWAA TQITISYTVV PFVLLSINPS FTFYRSWYYC
460 470 480 490 500
LHICSILVLL LLPVKKSPRK KNTEENAQPS WAKKFDEREN SLGQNSFSMM
510
NNVCNQNQDT GSRHSALTQ
Length:519
Mass (Da):59,001
Last modified:January 23, 2007 - v2
Checksum:iD5CAFBD16F7642B3
GO

Sequence cautioni

The sequence BC101889 differs from that shown. Reason: Frameshift at position 41. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03049793 Genomic DNA. No translation available.
AABR03054282 Genomic DNA. No translation available.
AABR03052483 Genomic DNA. No translation available.
AABR03050975 Genomic DNA. No translation available.
AABR03049616 Genomic DNA. No translation available.
BC101889 mRNA. No translation available.
RefSeqiNP_001101486.2. NM_001108016.2.
UniGeneiRn.35322.

Genome annotation databases

GeneIDi313997.
KEGGirno:313997.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03049793 Genomic DNA. No translation available.
AABR03054282 Genomic DNA. No translation available.
AABR03052483 Genomic DNA. No translation available.
AABR03050975 Genomic DNA. No translation available.
AABR03049616 Genomic DNA. No translation available.
BC101889 mRNA. No translation available.
RefSeqiNP_001101486.2. NM_001108016.2.
UniGeneiRn.35322.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009018.

Proteomic databases

PaxDbiQ3T1J2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi313997.
KEGGirno:313997.

Organism-specific databases

CTDi129642.
RGDi1305798. Mboat2.

Phylogenomic databases

eggNOGiCOG5202.
HOGENOMiHOG000015994.
HOVERGENiHBG058823.
InParanoidiQ3T1J2.
KOiK13517.
OrthoDBiEOG73Z2SW.
PhylomeDBiQ3T1J2.
TreeFamiTF314906.

Enzyme and pathway databases

UniPathwayiUPA00085.
ReactomeiREACT_339882. Acyl chain remodelling of PE.
REACT_341560. Acyl chain remodelling of PC.

Miscellaneous databases

NextBioi667109.
PROiQ3T1J2.

Gene expression databases

ExpressionAtlasiQ3T1J2. baseline.
GenevestigatoriQ3T1J2.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.

Entry informationi

Entry nameiMBOA2_RAT
AccessioniPrimary (citable) accession number: Q3T1J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.